Pancreatic hydrolysis

Reaction of Tryptophane. — Harlay also recommends the use of tryptophane to identify a tryptic digestion. Several drops of saturated bromine water, added to the liquids resulting from a pancreatic hydrolysis, cause the formation of a reddish yellow... 

Figure 12.19 Simplified scheme of the pancreatic hydrolysis of structured lipids (top 1,3-diacylglycerols bottom human milk fat replacers).

To start the second step of the hydrolysis, 15 ml of pancreatin solution (5 mg/ml, hog pancreas 5X) in phosphate buffer was introduced in the bag and mixed with the products of pectic digestion. Pancreatic hydrolysis products then were continuously collected as they were dialyzed for various periods of up to 24 hours. The amount of nitrogen released was determined by an Auto Analyzer (using the method no 329-74 W/B of Technicon, Tarrytown, N.Y.). Samples of dialysate and undigested protein fractions were hydrolyzed for 24 h in 6 N HCl at lOO C. Amino acid content was evaluated by high performance liquid chromatography (Vachon al., 1982). 

FIGURE 11.32 All example of nuclease specificity The specificity of RNA hydrolysis by bovine pancreatic RNase. This RNase cleaves h at 3 -pyriinidines, yielding oligonncleoddes with pyrimidine 3 -P04 ends. 

FIGURE 24.3 (a) A duct at the junction of the pancreas and duodenum secretes pancreatic juice into the duodenum, the first portion of the small intestine, (b) Hydrolysis of triacylglycerols by pancreatic and intestinal lipases. Pancreatic lipases cleave fatty acids at the C-1 and C-3 positions. Resulting monoacylglycerols with fatty acids at C-2 are hydrolyzed by intestinal lipases. Fatty acids and monoacylglycerols are absorbed through the intestinal wall and assembled into lipoprotein aggregates termed chylomicrons (discussed in Chapter 25). 

Elastase-like proteinases are serine proteinases that recognized peptide residues with linear aliphatic side chains (alanyl, valyl, leucyl or isoleucyl residues) and that effect hydrolysis of the polypeptide chain on the carboxy-terminal side of these residues. Examples of elastase-like proteinase are pancreatic elastase, neutrophil elastase and proteinase-3. 

The hydrolysis of starch by salivary and pancreatic amylases catalyze random hydrolysis of a(l—>4) glycoside bonds, yielding dextrins, then a mixmre of glucose, maltose, and isomaltose (from the branch points in amylopectin). 

There are two main classes of proteolytic digestive enzymes (proteases), with different specificities for the amino acids forming the peptide bond to be hydrolyzed. Endopeptidases hydrolyze peptide bonds between specific amino acids throughout the molecule. They are the first enzymes to act, yielding a larger number of smaller fragments, eg, pepsin in the gastric juice and trypsin, chymotrypsin, and elastase secreted into the small intestine by the pancreas. Exopeptidases catalyze the hydrolysis of peptide bonds, one at a time, fi"om the ends of polypeptides. Carboxypeptidases, secreted in the pancreatic juice, release amino acids from rhe free carboxyl terminal, and aminopeptidases, secreted by the intestinal mucosal cells, release amino acids from the amino terminal. Dipeptides, which are not substrates for exopeptidases, are hydrolyzed in the brush border of intestinal mucosal cells by dipeptidases. 

Hydrolysis of RNA by alkali or pancreatic RNase leads initially to fragments which terminate in 2, 3 -cyclic phosphodiesters. Micrococcal nuclease, on the other hand, gives rise to fragments terminating in 3 -phos-phomonoester groups which facilitate their isolation, and this enzymic hydrolysis has been used to prepare 3 -ribodinucleotides. ... 

Immobilized PLE was applied to promote stereoselective acetylation of prochiral bis(hydroxymethyl)methyl-phenylgermane 106 (R = Me) with vinyl acetate as a solvent and acyl donor. Later on, the same group reported that each enantiomer of hydridogermane monoacetates 107 (R = H) was obtained either via acetylation of the bis-hydroxy derivative 106 (R = H) or hydrolysis of the corresponding diacetate 108 (R = H). In both methods, porcine pancreatic lipase was used and, obviously, each reaction led to a different enantiomer of 107 (Equation 51). ... 

A. indica L. Indian Aristolochia, also known as Indian birthwort, ishvara (Sanskrit), or adagam (Tamil), is a bitter climber native to India. The medicinal material consists of the rhizome, which is to resolve inflammation (India), counteract insect poison, and as an antipyretic (Philippines and Vietnam). The rhizome contains aristolochic acid, which inhibits in vitro and dose-dependent phospholipid hydrolysis by the human synovial fluid phospholipase A2, snake venom phospholipase A2, porcine pancreatic phospholipase A2, and human platelet phospholipase A2 (2). 

The key-step of Mori s synthesis of 12 was pig pancreatic lipase (PPL)-cat-alyzed asymmetric hydrolysis of raeso-diacetate A to give B (Scheme 22) [32]. Purification of B (90.8% ee) afforded pure C, which was converted to 12. 

The absorption efficiency of the different carotenoids is variable. For example, (3-cryptoxanthin has been reported to have higher absorption efficiency than a-cryptoxanthin in rats (Breithaupt and others 2007). Carotenoids must be liberated from the food before they can be absorbed by intestinal cells (Faulks and Southon 2005). Mechanical disruption of the food by mastication, ingestion, and mixing leads to carotenoid liberation (Guyton and Hall 2001). The enzymatic and acid-mediated hydrolysis of carbohydrates, lipids, and proteins (chemical breaking of the food) also contributes to carotenoids liberation from the food matrix (Faulks and Southon 2005). Once released, carotenoids must be dissolved in oil droplets, which are emulsified with the aqueous components of the chyme. When these oil droplets are mixed with bile in the small intestine, their size is reduced, facilitating the hydrolytic processing of lipids by the pancreatic enzymes (Pasquier and others 1996 Furr and Clark 1997 ... 

The answer is b. (Hardman, pp 1268-1269J Asparaginase is an enzyme that catalyzes the hydrolysis of serum asparagine to aspartic acid and ammonia. Major toxicities are related to antigenicity and pancreatitis. In addition, more than 50% of those treated present biochemical evidence of hepatic dysfunction. 

The presence or absence of pancreatic enzymes can only be satisfactorily decided by intraduodenal intubation and direct examination of samples of small intestinal contents after the administration of a suitable stimulus to pancreatic secretion (Fll). It is not sufficient to look at one enzyme only, such as trypsin, since a specific deficiency of lipase can occur (Sll). Assessment of the degree of hydrolysis of fat in the stools is quite unreliable as a guide to pancreatic enzyme activity (CIO). 

Alpha amylases cause a rapid fragmentation of starch with an accompanying marked decrease in viscosity of the starch solutions. Therefore, viscosity determinations may be used to follow the early stages in the hydrolysis of starch by these amylases. Afthough this type of measurement is of considerable importance for certain industrial applications, it has not been used to any great extent in investigations with pancreatic amylase. 

The ratio of dextrinogenic to saccharogenic activities for pancreatic amylase, measured with Lintner s soluble potato starch under comparable conditions at 40°, is approximately 2 to 45,57 The achroic point is reached in the hydrolysis of potato starch by highly purified pancreatic amylase when approximately 20% of the glucose linkages of the starch have been broken.41... 

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